Phospholipase A2 - Vipera ammodytes meridionalis (Eastern sand viper)

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Reviewed, UniProtKB/Swiss-Prot P14420 (PA21B_VIPAE)

Last modified June 16, 2009. Version 79. History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein names	Recommended name: Phospholipase A2 EC=3.1.1.4 Alternative name(s): Phosphatidylcholine 2-acylhydrolase Vipoxin non-toxic component Vipoxin B chain
Organism	Vipera ammodytes meridionalis (Eastern sand viper)
Taxonomic identifier	73841 [NCBI]
Taxonomic lineage	Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Lepidosauria › Squamata › Scleroglossa › Serpentes › Colubroidea › Viperidae › Viperinae › Vipera

Protein attributes

Sequence length	122 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	PA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides. The vipoxin complex show postsynaptic neurotoxicity, while the isolated phospholipase A2 is a presynaptic neurotoxin.
Catalytic activity	Phosphatidylcholine + H₂O = 1-acylglycerophosphocholine + a carboxylate.
Cofactor	Binds 1 calcium ion per subunit By similarity.
Subunit structure	The main toxin of this snake venom is vipoxin, a complex of a toxic basic protein (B chain) having phospholipase A2 activity and a nontoxic acidic protein (A chain) functioning as its inhibitor. Without the inhibitor, the basic protein becomes unstable and within 12-14 days loses its enzymatic activity.
Subcellular location	Secreted.
Tissue specificity	Expressed by the venom gland.
Miscellaneous	The supposed calcium binding region close to Asp-48 of the basic phospholipase A2 is blocked by the side chain of Lys-60 of its inhibitor.
Sequence similarities	Belongs to the phospholipase A2 family. Group II subfamily.

Ontologies

Keywords
Biological process	Lipid degradation
Cellular component	Secreted
Ligand	Calcium Metal-binding
Molecular function	Hydrolase Neurotoxin Postsynaptic neurotoxin Presynaptic neurotoxin Toxin
PTM	Disulfide bond
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological process	lipid catabolic process Inferred from electronic annotation. Source: UniProtKB-KW pathogenesis Inferred from electronic annotation. Source: UniProtKB-KW phospholipid metabolic process Inferred from electronic annotation. Source: InterPro synaptic transmission Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell postsynaptic membrane Inferred from electronic annotation. Source: UniProtKB-KW presynaptic membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	acetylcholine receptor inhibitor activity Inferred from electronic annotation. Source: UniProtKB-KW calcium ion binding Inferred from electronic annotation. Source: UniProtKB-KW phospholipase A2 activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

122

Phospholipase A2

PRO_0000161712

Sites

Active site

1

By similarity

Active site

1

By similarity

Metal binding

1

Calcium; via carbonyl oxygen By similarity

Metal binding

1

Calcium; via carbonyl oxygen By similarity

Metal binding

1

Calcium; via carbonyl oxygen By similarity

Metal binding

1

Calcium By similarity

Amino acid modifications

Disulfide bond

Disulfide bond

Disulfide bond

Disulfide bond

Disulfide bond

Disulfide bond

Disulfide bond

Secondary structure

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122

Helix Strand Turn

Sequences

Sequence

Length

Mass (Da)

Tools

P14420-1 [UniParc].

Last modified January 1, 1990. Version 1.
Checksum: 94438F9F1285FC7D
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122

13,828

        10         20         30         40         50         60 
NLFQFAKMIN GKLGAFSVWN YISYGCYCGW GGQGTPKDAT DRCCFVHDCC YGRVRGCNPK 

        70         80         90        100        110        120 
LAIYSYSFKK GNIVCGKNNG CLRDICECDR VAANCFHQNK NTYNKNYKFL SSSRCRQTSE 


QC

References

[1]	"Sequence homology between phospholipase and its inhibitor in snake venom. The primary structure of phospholipase A2 of vipoxin from the venom of the Bulgarian viper (Vipera ammodytes ammodytes, Serpentes)." Mancheva I., Kleinschmidt T., Aleksiev B., Braunitzer G. Biol. Chem. Hoppe-Seyler 368:343-352(1987) [PubMed: 3606821] [Abstract] Cited for: PROTEIN SEQUENCE. Strain: Bulgarian. Tissue: Venom.
[2]	"Crystals of phospholipase A2 inhibitor. The non-toxic component of vipoxin from the venom of Bulgarian viper (Vipera ammodytes)." Devedjiev Y., Atanasov B., Mancheva I., Aleksiev B. J. Mol. Biol. 229:1147-1149(1993) [PubMed: 8445639] [Abstract] Cited for: CRYSTALLIZATION. Tissue: Venom.
[3]	"Crystallization and preliminary X-ray analysis of vipoxin, a complex between a toxic phospholipase A2 and its natural polypeptide inhibitor." Betzel C., Visanji M., Wilson K.S., Genov N., Mancheva I., Aleksiev B., Singh T.P. J. Mol. Biol. 231:498-500(1993) [PubMed: 8510159] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS). Tissue: Venom.
[4]	"Crystal structure of vipoxin at 2.0 A: an example of regulation of a toxic function generated by molecular evolution." Perbandt M., Wilson J.C., Eschenburg S., Mancheva I., Aleksiev B., Genov N., Willingmann P., Weber W., Singh T.P., Betzel C. FEBS Lett. 412:573-577(1997) [PubMed: 9276469] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2 ANGSTROMS).
[5]	"Structure of the neurotoxic complex vipoxin at 1.4 A resolution." Banumathi S., Rajashankar K.R., Notzel C., Aleksiev B., Singh T.P., Genov N., Betzel C. Acta Crystallogr. D 57:1552-1559(2001) [PubMed: 11679719] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS).
+	Additional computationally mapped references.

Cross-references

Sequence databases

PIR

3D structure databases

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1AOK	X-ray	2.00	B	1-118	[»]
1JLT	X-ray	1.40	B	1-122	[»]
1RGB	X-ray	3.30	A/B/K/L	1-122	[»]

ModBase

Phylogenomic databases

HOVERGEN

Enzyme and pathway databases

BRENDA

3.1.1.4. 294522.

Family and domain databases

InterPro

IPR016090. Phospholipase_A2.
IPR013090. Phospholipase_A2_AS.
IPR001211. Phospholipase_A2_euk.
[Graphical view]

Gene3D

G3DSA:1.20.90.10. Phospholipase_A2. 1 hit.

PANTHER

PTHR11716. Phospholipase_A2. 1 hit.

Pfam

PF00068. Phospholip_A2_1. 1 hit.
[Graphical view]

PRINTS

PR00389. PHPHLIPASEA2.

ProDom

PD000303. PhospholipaseA2. 1 hit.
[Graphical view] [Entries sharing at least one domain]

SMART

SM00085. PA2c. 1 hit.
[Graphical view]

PROSITE

PS00119. PA2_ASP. 1 hit.
PS00118. PA2_HIS. 1 hit.
[Graphical view]

ProtoNet

Entry information

Entry name

PA21B_VIPAE

Accession

Primary (citable) accession number: P14420

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 1, 1990
Last sequence update:	January 1, 1990
Last modified:	June 16, 2009
This is version 79 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents